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首页> 外文期刊>Journal of Molecular Biology >Kinetic mechanism of end-to-end annealing of actin filaments
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Kinetic mechanism of end-to-end annealing of actin filaments

机译：肌动蛋白丝端对端退火的动力学机理

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We investigated the effect of actin filament length and capping protein on the rate of end-to-end annealing of actin filaments. Long filaments were fragmented by shearing and allowed to recover. Stabilizing filaments with phalloidin in most experiments eliminated any contribution of subunit dissociation and association to the redistribution of lengths but did not affect the results. Two different assays, fluorescence microscopy to measure filament lengths and polymerization to measure concentration of barbed filament ends, gave the same time-course of annealing. The rate of annealing declines with time as the average filament length increases. Longer filaments also anneal slower than short filaments. The second-order annealing rate constant is inversely proportional to mean polymer length with a value of 1.1 nM(-1) s(-1)/length in subunits. Capping protein slows but does not prevent annealing. Annealing is a highly favorable reaction with a strong influence on the length of polymers produced by spontaneous polymerization and should be considered in thinking about polymer dynamics in cells.
机译：我们研究了肌动蛋白丝长度和封端蛋白对肌动蛋白丝端对端退火速率的影响。通过剪切使长丝碎裂并使其恢复。在大多数实验中，用鬼笔环肽稳定细丝可以消除亚基解离和缔合长度重新分布的任何作用，但不会影响结果。两种不同的测定法，即荧光显微镜法测定长丝长度和聚合法测定带刺长丝末端的浓度，给出了相同的退火时间。随着平均长丝长度的增加，退火速率随时间下降。长丝的退火也比短丝的退火慢。二阶退火速率常数与平均聚合物长度成反比，平均长度为1.1 nM（-1）s（-1）/单位为亚单位。封端蛋白减慢但不能阻止退火。退火是非常有利的反应，对自发聚合产生的聚合物的长度有很大的影响，在考虑细胞中的聚合物动力学时应考虑退火。

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